6SBT

Structure of GluK1 ligand-binding domain (S1S2) in complex with N-(7-(1H-imidazol-1-yl)-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl benzamide at 2.3 A resolution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0015276	molecular_function	ligand-gated monoatomic ion channel activity
A	0016020	cellular_component	membrane

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	binding site for residue SO4 A 301

Chain	Residue
A	GLY140
A	SER141
A	THR142
A	MET189
A	GLU190
A	L5H303
A	HOH409

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site_id	AC2
Number of Residues	2
Details	binding site for residue SO4 A 302

Chain	Residue
A	ARG31
A	LYS54

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site_id	AC3
Number of Residues	13
Details	binding site for residue L5H A 303

Chain	Residue
A	GLU13
A	TYR16
A	TYR61
A	PRO88
A	LEU89
A	THR90
A	ARG95
A	ASP139
A	THR144
A	TYR216
A	SO4301
A	CL304
A	HOH445

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site_id	AC4
Number of Residues	2
Details	binding site for residue CL A 304

Chain	Residue
A	THR90
A	L5H303

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site_id	AC5
Number of Residues	3
Details	binding site for residue GOL A 306

Chain	Residue
A	ASP212
A	SER213
A	HIS244

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site_id	AC6
Number of Residues	5
Details	binding site for residue GOL A 307

Chain	Residue
A	GLU13
A	GLU14
A	GLU175
A	HOH416
A	HOH443

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:15710405, ECO:0007744|PDB:1YCJ

Chain	Residue	Details
A	LYS103
A	PHE105
A	LYS156
A	MET157

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site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:15710405, ECO:0000269|PubMed:15721240, ECO:0007744|PDB:1YCJ

Chain	Residue	Details
A	ILE110
A	THR205

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphoserine; by PKC => ECO:0000255

Chain	Residue	Details
A	ILE177

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphothreonine; by PKC => ECO:0000255

Chain	Residue	Details
A	SER213

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site_id	SWS_FT_FI5
Number of Residues	3
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	ILE11
A	MET18
A	VAL218

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